Welcome to the Purvis Lab.  

In hope of one day securing some real lab space, purvislab.org has become a virtual home to the various projects and personalities I've encountered during my lifetime in Academia. It also allows me to shamelessly promote myself while searching for a postdoc.

Most of my research efforts involve some type of computational approach to understanding signal transduction in biological systems. Specifically, our work has led to insights into human platelet activation and oncogenic signaling via the epidermal growth factor receptor. A long-term goal is to use these computational techniques to generate accurate, quantitative models of signaling systems that may be used to design patient-specific therapies.

My modern inspirations include work by Michael Yaffe, Kevin Janes, Doug Lauffenburger, Boris Kholodenko, and many others. Older inspirations include giants like Gauss and Fourier.

SEE RELATED :
Friends and colleagues | some short biosketches
Diamond Lab | blood biology and drug discovery at UPenn
Radhakrishnan Lab | multiscale modeling lab at UPenn
Brass Lab | platelet signaling lab at UPenn
Ingram Lab | metabolic engineering lab at UF
 
Latest PubMed search results for "systems biology"  
Empirically controlled mapping of t... Nat Methods
Developmental stages until hatching... J Morphol
Watershed land use as a determinant... Environ Geochem Health
Chapter 6 new insights into melanos... Int Rev Cell Mol Biol
An EGF-like peptide sequence from D... Biochem Biophys Res Commun
 
Platelet Signaling Model  
We have assembled a quantitative, molecular model of platelet rest and activation. Currently, the model includes a single receptor, reactions to handle phosphoinositide metabolism and calcium regulation, and a negative feedback loop exerted through protein kinase C. The model will eventually be incorporated into larger scale models of blood coagulation under flow.  
SEE RELATED :
bloodsystemsbiology.org
Systems Biology Markup Language (SBML)
PubMed
 
   
Inhibition model for EGFR signaling  
By modeling multiple, distinct phosphorylation sites on the epidermal growth factor receptor (EGFR) cytoplasmic tail, we show how altered phosphorylation kinetics of a oncogenic form of the receptor can lead to increased drug sensitivity.  
   
Engineering osmotolerance in E. coli  
In this study, we engineered a strain of E. coli to overproduce trehalose, an important osmoprotectant and stress protectant synthesized by many organisms. Integration of an inducible otsBA operon was used to increase the growth of E. coli in the presence of a variety of osmotic-stress agents, such as sugars and salts. Based on these results, overproduction of trehalose may be a useful trait to include in biocatalysts engineered for commodity chemicals.